Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
4 L-ascorbate + O2 | Cucurbita pepo | - |
4 monodehydroascorbate + 2 H2O | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Cucurbita pepo | - |
subsp. pepo convar. giromontiina | - |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
fruit | - |
Cucurbita pepo | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
4 L-ascorbate + O2 | - |
Cucurbita pepo | 4 monodehydroascorbate + 2 H2O | - |
? |
Subunits | Comment | Organism |
---|---|---|
homodimer | ascorbate oxidase is a large, multidomain, dimeric protein | Cucurbita pepo |
More | structure analysis: the monomers keep their secondary structure, whereas subtle conformational changes in the tertiary structure become apparent, salt bridges and electrostatic interactions occurring at the dimeric interface play a crucial role in the stabilization of the monomer's tertiary structure., folding/unfolding pathway, overview. Each subunit is formed by three distinct domains and contains four copper ions, three of which are located at the interface between domains, forming a so-called trinuclear centre | Cucurbita pepo |
Synonyms | Comment | Organism |
---|---|---|
AAO | - |
Cucurbita pepo |
ascorbate oxidase | - |
Cucurbita pepo |
General Information | Comment | Organism |
---|---|---|
additional information | partially folded monomeric species might populate the energy landscape of the enzyme. The overall AAO stability is crucially controlled by a few quaternary interactions at the subunits' interface | Cucurbita pepo |